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J. Biol. Chem., Vol. 255, Issue 22, 10569-10571, 11, 1980

Repair of alkylated DNA in Escherichia coli. Methyl group transfer from O6-methylguanine to a protein cysteine residue

M Olsson and T Lindahl

O6-Methylguanine residues disappear from alkylated DNA by an inducible repair process in Escherichia coli. The reaction can be studied in a cell-free system, using DNA treated with a radioactive methylating agent as substrate. The disappearance of labeled O6-methylguanine from DNA is not accompanied by release of radioactive material in an acid- soluble form. Instead, the methyl group of O6-methylguanine appears to be transferred enzymatically to a protein cysteine residue. Radioactively labeled S-methylcysteine has been identified in protein hydrolysates after incubation of the alkylated DNA with a partly purified E. coli methyltransferase activity. The radioactive amino acid residue shows properties identical with those of S-methylcysteine by automatic amino acid analysis and paper chromatography in several solvent systems. Moreover, oxidation of the compound with hydrogen peroxide yields a product which co-chromatographs with S-methylcysteine sulfone.
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